MYO7B_MOUSE
ID MYO7B_MOUSE Reviewed; 2113 AA.
AC Q99MZ6; B9EHR5; Q571N7; Q8R0U3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Unconventional myosin-VIIb;
GN Name=Myo7b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Inner ear, and Kidney;
RX PubMed=11401444; DOI=10.1006/geno.2000.6456;
RA Chen Z.-Y., Hasson T., Zhang D.-S., Schwender B.J., Derfler B.H.,
RA Mooseker M.S., Corey D.P.;
RT "Myosin-VIIb, a novel unconventional myosin, is a constituent of microvilli
RT in transporting epithelia.";
RL Genomics 72:285-296(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1114-2113.
RC TISSUE=Embryonic intestine;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904; THR-1339; SER-1368 AND
RP SER-1642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24725409; DOI=10.1016/j.cell.2014.01.067;
RA Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E.,
RA Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A.,
RA Kachar B., Tyska M.J.;
RT "Intestinal brush border assembly driven by protocadherin-based
RT intermicrovillar adhesion.";
RL Cell 157:433-446(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 962-1578 IN COMPLEX WITH ANKS4B,
RP AND REGION.
RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
RA Li J., He Y., Lu Q., Zhang M.;
RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush
RT border microvilli tip-link complex.";
RL Dev. Cell 36:179-189(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments. As part
CC of the intermicrovillar adhesion complex/IMAC plays a role in
CC epithelial brush border differentiation, controlling microvilli
CC organization and length. May link the complex to the actin core bundle
CC of microvilli. {ECO:0000250|UniProtKB:Q6PIF6}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5. Interacts with CDHR2. Interacts with CDHR5.
CC Interacts with USH1C (By similarity). Interacts with ANKS4B; requires
CC initial interaction with USH1C (Probable).
CC {ECO:0000250|UniProtKB:Q6PIF6, ECO:0000305|PubMed:26812017}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:11401444}. Cell projection, microvillus
CC {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}.
CC Note=Enriched in the microvilli of the intestinal brush border.
CC {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in kidney and intestine.
CC Detected in proximal tubule cells of the kidney and enterocytes of the
CC intestine, specifically the distal tips of apical microvilli on these
CC transporting epithelial cells (at protein level).
CC {ECO:0000269|PubMed:11401444, ECO:0000269|PubMed:24725409}.
CC -!- DEVELOPMENTAL STAGE: Detected in intestinal enterocytes at embryonic
CC day 17. {ECO:0000269|PubMed:11401444}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-7 (MYH7). {ECO:0000305}.
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DR EMBL; AF242411; AAK28339.1; -; mRNA.
DR EMBL; BC138338; AAI38339.1; -; mRNA.
DR EMBL; BC138341; AAI38342.1; -; mRNA.
DR EMBL; BC026416; AAH26416.1; -; mRNA.
DR EMBL; AK220152; BAD90338.1; -; mRNA.
DR CCDS; CCDS50244.1; -.
DR RefSeq; NP_115770.2; NM_032394.3.
DR PDB; 5F3Y; X-ray; 3.41 A; A=962-1578.
DR PDBsum; 5F3Y; -.
DR AlphaFoldDB; Q99MZ6; -.
DR SMR; Q99MZ6; -.
DR STRING; 10090.ENSMUSP00000118046; -.
DR iPTMnet; Q99MZ6; -.
DR PhosphoSitePlus; Q99MZ6; -.
DR jPOST; Q99MZ6; -.
DR MaxQB; Q99MZ6; -.
DR PaxDb; Q99MZ6; -.
DR PeptideAtlas; Q99MZ6; -.
DR PRIDE; Q99MZ6; -.
DR ProteomicsDB; 286131; -.
DR Antibodypedia; 47564; 27 antibodies from 17 providers.
DR DNASU; 17922; -.
DR Ensembl; ENSMUST00000134663; ENSMUSP00000118046; ENSMUSG00000024388.
DR GeneID; 17922; -.
DR KEGG; mmu:17922; -.
DR UCSC; uc008eix.2; mouse.
DR CTD; 4648; -.
DR MGI; MGI:107709; Myo7b.
DR VEuPathDB; HostDB:ENSMUSG00000024388; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000157247; -.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q99MZ6; -.
DR OMA; TLGIADM; -.
DR OrthoDB; 527681at2759; -.
DR PhylomeDB; Q99MZ6; -.
DR TreeFam; TF335306; -.
DR BioGRID-ORCS; 17922; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q99MZ6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q99MZ6; protein.
DR Bgee; ENSMUSG00000024388; Expressed in intestinal villus and 47 other tissues.
DR Genevisible; Q99MZ6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0090651; C:apical cytoplasm; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:1904970; P:brush border assembly; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 1.25.40.530; -; 3.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Differentiation; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2113
FT /note="Unconventional myosin-VIIb"
FT /id="PRO_0000329047"
FT DOMAIN 65..760
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 745..765
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 763..792
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 786..815
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 809..838
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 832..861
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 855..884
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 989..1189
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1194..1503
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1498..1564
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1641..1790
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1790..1896
FT /note="MyTH4 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1796..2099
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 637..659
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 962..1578
FT /note="Mediates interaction with ANKS4B"
FT /evidence="ECO:0000269|PubMed:26812017"
FT REGION 1497..2113
FT /note="Mediates interaction with CDHR2, CDHR5 and USH1C"
FT /evidence="ECO:0000250|UniProtKB:Q6PIF6"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1339
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 227..228
FT /note="IE -> LA (in Ref. 1; AAK28339)"
FT /evidence="ECO:0000305"
FT CONFLICT 2033
FT /note="L -> V (in Ref. 1; AAK28339)"
FT /evidence="ECO:0000305"
FT HELIX 973..980
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1006..1020
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1086..1099
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1103..1115
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1121..1137
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1142..1144
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1145..1153
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1157..1159
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1160..1173
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1182..1190
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1194..1200
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1205..1210
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1216..1227
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1235..1241
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1244..1247
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1249..1252
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1255..1269
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1273..1275
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1278..1284
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1297..1313
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1314..1316
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1321..1335
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1342..1352
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1355..1358
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1363..1377
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1378..1380
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1386..1400
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1402..1405
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1406..1415
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1422..1428
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1433..1436
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1442..1446
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1448..1450
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1451..1456
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1465..1472
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1474..1478
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1482..1499
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1502..1505
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1525..1527
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1537..1545
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 1546..1548
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1551..1555
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1556..1558
FT /evidence="ECO:0007829|PDB:5F3Y"
FT STRAND 1559..1561
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 1570..1575
FT /evidence="ECO:0007829|PDB:5F3Y"
SQ SEQUENCE 2113 AA; 240859 MW; 7116B047D1B08AA7 CRC64;
MSVFRLGDHV WLDPPSSSKT GVAIGGIVKE TKLGKTLIED DEGKEHWVHA EDLSTLRPMH
PNSAQGVDDM IRLGDLNEAG VVHNLLIRYQ QHKIYTYTGS ILVAVNPFQM LPLYTLEQVQ
IYYSRHMGEL PPHIFAIANS CYFNMKKNKR DQCCIISGES GAGKTETTKL ILQFLATVSG
QHSWIEQQVL EANPILEAFG NAKTIRNDNS SRFGKYIDIH FNSSGVIEGA SIEHFLLEKS
RVCRQAPEER NYHIFYCMLM GMSPEEKQML SLGMPSEYHY LTMGSCTSSE GLSDAKDYAH
VRSAMKILQF SDSENWDISK LLAAILHLGN VGFMAAVFEN LDSSDVMETP AFPLAMKLLE
VQHQALRDCL IKHTIPVLGE FVSRPVNIAQ ATDRRDAFVK GIYGRLFQWI VKKINAAIFT
PQAQDPQNVR RAIGLLDIFG FENFQNNSFE QLCINFANEH LQQFFVKHVF TMEQEEYLSE
NITWNYIHYT DNQPILDMLA LKPMSIISLL DEESRFPQGT DVTMLQKLNS IHANNKSFLS
PRSIHDTRFG IAHFAGDVYY QAEGFLEKNR DVLSTDILIL IHSSKNKFLK EIFNVDSSQT
KLGHGTICQV KAGSQLFKSS DSIKRPVTLA SQFKQSLDQL MRILTNCQPY FVRCIKPNEY
KKPLLFDREL CIQQLRYSGM METVHIRKSG FPIRYTFDEF SQRFRVLLPS PERMQFQNKP
RQMTLHIADL CLGTDKDWKV GKTKIFLKDH QDTVLEIRRS QALDGAAIRI QRVLRGHKYR
KEFLRQRRAA VTLQAGWRGY SQRKNFKLIL VGFERLQAIA RSHLLMRQFQ AMRQRIVQLQ
ARCRGYLVRQ QVQAKRRAVV IIQAHARGMV VRKSYWQQKS TGPQVILAKE PKAQVAVHER
KRKSIYDTVT DTAMVEKVFG FLPAMIGGQE GPAPTRFEDL EVKTQKLHEV DLDTVPMMAM
PEEEVDSLAE YTFPKFAVTY FQKSASHTHI QKPLRYPLLY HENDTDHSAA LDVWIIILRF
MGDLPEPVVY GRNSLTGSSV MRQIHDKLGK DSVTQHNRSS QVASQLNFGE EAFKFDGPIS
DRPMSNLEKV HFIVGYAIMR PGLRDEIYCQ ICKQLSENYK TSSRARGWIL LSLCLGCFPP
SERFMKYLLN FISQGPPSYG PFCAERLQRT FANGVRAEPP TWLELQAVKS KKHIPIQVIL
ATGRSLTISV DSASTSREIC QHVAQKQGLR DNLGFSLQVA VYDKFWSLGS GCDHLMDAVA
QCEQLARERG ESQRQAPWRI YFRKEFFTPW HDSQEDPVST ELIYHQVLRG VWSGEYNFEK
EEELVELLAR HCYVQLGATV KSNAVQELLP SCVPSKLYRT KSPEKWASLV TAAHAKAQYT
QSKATPLAVR EQTVEAARLL WPLLFSRLFE VTTLSGPRLP KTQLVLAINW KGMYFLDQKE
RTLLGLSFAE VMGLVANRDA PGGKKLLLAT LQEEYEFVSP SSVAIAEMVA LFLGGLKERS
VFAMALQDRR ATDDITLLPF KKGDLLILTK KQGLLASENW ALGQNDRTGK TGLVPTACLY
TIPSVTKPST QLLSLLAMSP EKRKLAAQEV RALEPPLEDQ LTESPYTLEE FSYQFFRAPE
KETISRAAMP MARSRGHLWA YSPEPLRQPL LKSVHDKAKL RDAACQIFLA ILKYTGDYPS
RQSWHSLELT DQMFSLALQD PALQDELYCQ ILKQLTHNSI RFSEERAWQL LWLCTGLFPP
GKTLLPHAQK FIDSRKKKPL ALDCSRRLHR VLRVGPRKQP PHDVEVKAAE QNVSKLHHEV
YLPNDTSKSM EVGSSSRVRD LCEGIGTRLQ LASWDGCSLF IKITDKVISL KEGDFFFDSL
RQVSDWVKKN RPQKEGASVT LPYQVFFMRK LWLNVTPGKD VNADTILHYH QELPKYLRGF
HKCSREDAIH LGGLICKIQF GSDSSQLASV SKVLKELVPQ NLTRLMSSEE WKKSLLLECD
KNKRKTVAEA KVEFLKYMYR WPTFGSAFFE VKQTSEPSYP DILLIAINRH GLLLIHPKTK
ELLNTYPFTK ISSWSSGNTY FHMALGSLGQ GSRLLCETSL GYKMDDLLTS YVQQLLNTVN
KQRGFRAPAP ANP
